ACTION OF A BACTERIAL AGARASE ON AGAROSE PORPHYRAN AND ALKALI-TREATED PROPHYRAN
ACTION OF A BACTERIAL AGARASE ON AGAROSE PORPHYRAN AND ALKALI-TREATED PROPHYRAN
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DOI:
10.1042/bj1130687
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发表时间:
1969-01-01
影响因子:
4.1
通讯作者:
TURVEY, JR
中科院分区:
文献类型:
--
作者:
DUCKWORTH, M;TURVEY, JR
1. A purified extracellular agarase from aCytophagaspecies was used to hydrolyse agarose, porphyran and alkali-treated porphyran. 2. The hydrolysate from agarose was separated by gel filtration into the series of neoagarosaccharides, the predominant member of which was the tetrasaccharide. 3. Enzyme action on alkali-treated porphyran gave neoagarosaccharides and other oligosaccharides containing 6-O-methyl-d-galactose units. From the composition of these oligosaccharides it is deduced that action of the enzyme on ad-galactosidic linkage is four to five times faster than on the 6-O-methyl-d-galactosidic linkage. 4. Enzyme action on native porphyran gives a similar series of oligosaccharides but in smaller yield, much of the polysaccharide being either not degraded or only degraded to a series of large, highly sulphated oligosaccharides. 5. For porphyran, it is concluded that 6-O-methyl ether groups are distributed randomly on half thed-galactose units, but that the 6-sulphate groups onl-galactose units tend to occur in blocks.